ID   MSA2_PLAFZ              Reviewed;         300 AA.
AC   Q03645;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Merozoite surface antigen 2;
DE            Short=MSA-2;
DE   Flags: Precursor;
GN   Name=MSA2;
OS   Plasmodium falciparum (isolate mad71 / Papua New Guinea).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=70154;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2000383; DOI=10.1073/pnas.88.5.1751;
RA   Smythe J.A., Coppel R.L., Day K.P., Martin R.K., Oduola A.M.J., Kemp D.J.,
RA   Anders R.F.;
RT   "Structural diversity in the Plasmodium falciparum merozoite surface
RT   antigen 2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:1751-1755(1991).
CC   -!- FUNCTION: May play a role in the merozoite attachment to the
CC       erythrocyte.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC   -!- DEVELOPMENTAL STAGE: During the trophozoite and schizont stages.
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DR   EMBL; M59768; AAA29696.1; -; Genomic_DNA.
DR   PIR; A39112; A39112.
DR   AlphaFoldDB; Q03645; -.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   InterPro; IPR001136; MSA_2.
DR   Pfam; PF00985; MSA_2; 1.
DR   PIRSF; PIRSF003575; MSA_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Malaria; Membrane;
KW   Merozoite; Repeat; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..274
FT                   /note="Merozoite surface antigen 2"
FT                   /id="PRO_0000024604"
FT   PROPEP          275..300
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000024605"
FT   REGION          44..226
FT                   /note="Polymorphic region"
FT   REGION          111..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..255
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           274
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        22
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        249
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        273
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   300 AA;  30101 MW;  E4116107747AA10D CRC64;
     MKVIKTLSII NFFIFVTFNI KNESKYSNTF INNAYNMSIR RSMEESKPPT GAVAGSGAGA
     GSGAGAVAGS GAGAVAGSGA GAVAGSGAGA VAGSGAGAVA GSGAVAGSGA GNGANPGADA
     ERGPSTPATT TTTTTTNDAE ASTSTSSENR NHNNAETNPK GKGEVQKPNQ ANKETQNNSN
     VQQDSQTKSN VPRTQDADTK SPTAQPEQAE NSAPTAEQTE SPELQSAPEN KGTGQHGHMH
     GSRNNHPQNT SDSQKECTDG NKENCGAATS LLNNSSNIAS INKFVVLISA TLVLSFAIFI